1knz
From Proteopedia
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| - | [[Image:1knz.gif|left|200px]] | ||
| - | + | ==Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer== | |
| - | + | <StructureSection load='1knz' size='340' side='right'caption='[[1knz]], [[Resolution|resolution]] 2.45Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1knz]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Simian_rotavirus_A/SA11 Simian rotavirus A/SA11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KNZ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1knz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1knz OCA], [https://pdbe.org/1knz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1knz RCSB], [https://www.ebi.ac.uk/pdbsum/1knz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1knz ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | '' | + | [https://www.uniprot.org/uniprot/NSP3_ROTS1 NSP3_ROTS1] Involved in the shutoff of host protein synthesis. It is unclear whether it is required for the translation of viral mRNAs as well. Functions similarly to, and competes with the cellular poly(A)-binding protein PABPC1. Binds the conserved sequence 'GACC' at the 3' end of viral mRNAs and allows circularization of viral mRNAs in translation. Interacts with ZC3H7B/RoXaN and with the eukaryotic translation initiation factor eIF4G, using the same region employed by PABP-C1. NSP3 thus displaces PABPC1 from eIF4G, inhibiting the translation of cellular poly(A) mRNAs. Also responsible for the nuclear relocalization of PABPC1 upon rotavirus infection (By similarity). |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | == | + | Check<jmol> |
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/1knz_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1knz ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Rotaviruses, the cause of life-threatening diarrhea in humans and cattle, utilize a functional homolog of poly(A) binding protein (PABP) known as nonstructural protein 3 (NSP3) for translation of viral mRNAs. NSP3 binds to viral mRNA 3' consensus sequences and circularizes the mRNA via interactions with eIF4G. The X-ray structure of the NSP3 RNA binding domain bound to a rotaviral mRNA 3' end has been determined. NSP3 is a novel, heart-shaped homodimer with a medial RNA binding cleft. The homodimer is asymmetric, and contains two similar N-terminal segments plus two structurally different C-terminal segments that intertwine to create a tunnel enveloping the mRNA 3' end. Biophysical studies demonstrate high affinity binding leading to increased thermal stability and slow dissociation kinetics, consistent with NSP3 function. | Rotaviruses, the cause of life-threatening diarrhea in humans and cattle, utilize a functional homolog of poly(A) binding protein (PABP) known as nonstructural protein 3 (NSP3) for translation of viral mRNAs. NSP3 binds to viral mRNA 3' consensus sequences and circularizes the mRNA via interactions with eIF4G. The X-ray structure of the NSP3 RNA binding domain bound to a rotaviral mRNA 3' end has been determined. NSP3 is a novel, heart-shaped homodimer with a medial RNA binding cleft. The homodimer is asymmetric, and contains two similar N-terminal segments plus two structurally different C-terminal segments that intertwine to create a tunnel enveloping the mRNA 3' end. Biophysical studies demonstrate high affinity binding leading to increased thermal stability and slow dissociation kinetics, consistent with NSP3 function. | ||
| - | + | Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer.,Deo RC, Groft CM, Rajashankar KR, Burley SK Cell. 2002 Jan 11;108(1):71-81. PMID:11792322<ref>PMID:11792322</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1knz" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Nonstructural protein 3D structures|Nonstructural protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Simian rotavirus A/SA11]] | ||
| + | [[Category: Burley SK]] | ||
| + | [[Category: Deo RC]] | ||
| + | [[Category: Groft CM]] | ||
| + | [[Category: Rajashankar KR]] | ||
Current revision
Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer
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